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Membrane integration and topology of RIFIN and STEVOR proteins of the Plasmodium falciparum parasite
Author(s) -
Andersson Annika,
Kudva Renuka,
Magoulopoulou Anastasia,
Lejarre Quentin,
Lara Patricia,
Xu Peibo,
Goel Suchi,
Pissi Jennifer,
Ru Xing,
Hessa Tara,
Wahlgren Mats,
Heijne Gunnar,
Nilsson IngMarie,
TellgrenRoth Åsa
Publication year - 2020
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15171
Subject(s) - membrane protein , plasmodium falciparum , endoplasmic reticulum , biology , microbiology and biotechnology , membrane topology , plasmodium (life cycle) , open reading frame , parasite hosting , topology (electrical circuits) , membrane , gene , genetics , peptide sequence , malaria , immunology , mathematics , combinatorics , world wide web , computer science
The malarial parasite Plasmodium exports its own proteins to the cell surfaces of red blood cells (RBCs) during infection. Examples of exported proteins include members of the repetitive interspersed family (RIFIN) and subtelomeric variable open reading frame (STEVOR) family of proteins from Plasmodium falciparum . The presence of these parasite‐derived proteins on surfaces of infected RBCs triggers the adhesion of infected cells to uninfected cells (rosetting) and to the vascular endothelium potentially obstructing blood flow. While there is a fair amount of information on the localization of these proteins on the cell surfaces of RBCs, less is known about how they can be exported to the membrane and the topologies they can adopt during the process. The first step of export is plausibly the cotranslational insertion of proteins into the endoplasmic reticulum (ER) of the parasite, and here, we investigate the insertion of three RIFIN and two STEVOR proteins into the ER membrane. We employ a well‐established experimental system that uses N ‐linked glycosylation of sites within the protein as a measure to assess the extent of membrane insertion and the topology it assumes when inserted into the ER membrane. Our results indicate that for all the proteins tested, transmembranes (TMs) 1 and 3 integrate into the membrane, so that the protein assumes an overall topology of Ncyt‐Ccyt. We also show that the segment predicted to be TM2 for each of the proteins likely does not reside in the membrane, but is translocated to the lumen.